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SYR_PHOPR
ID   SYR_PHOPR               Reviewed;         576 AA.
AC   Q6LTA1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=PBPRA1064;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; CR378666; CAG19475.1; -; Genomic_DNA.
DR   RefSeq; WP_011217808.1; NC_006370.1.
DR   AlphaFoldDB; Q6LTA1; -.
DR   SMR; Q6LTA1; -.
DR   STRING; 298386.PBPRA1064; -.
DR   PRIDE; Q6LTA1; -.
DR   EnsemblBacteria; CAG19475; CAG19475; PBPRA1064.
DR   KEGG; ppr:PBPRA1064; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..576
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242064"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   576 AA;  64249 MW;  BB7B31D5B0E4BDED CRC64;
     MNIQALINDK VSQALEAAGA PAGSPAAVRQ SAKIQFGDYQ ANGVMGVAKK LGTNPREFAQ
     KVIDVLDLDG IAEKVEIAGP GFINIFLDKS WLAARAEEAL TDDRIGVAAE KQQNIVVDYS
     APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HNVVRANHIG DWGTQFGMLI ANLERVQNET
     GEVSMELADL EGFYRESKKL YDEDEEFAVR ARAFVVKLQS GDEYCAEMWK KLVDVTMVQN
     QINYDRLNVS LTRDNVMGES MYNYMLPGIV ADLKEKGLAV ESDGAQVVFL DEYKNKDGDP
     MGVIIQKRDG GFLYTTTDIA CAKYRFEQLN ADRVLYFIDS RQHQHLMQAW SIVRKAGYVP
     EEVTLEHHAF GMMLGKDGRP FKTRAGGTVR LADLLDESEV RAAKLIEAKN PDLDTAEKDK
     IAKTVAMAAV KYADLSKHRT TDYIFDWDNM LAFEGNTAPY MQYAYTRVAS IFKRADVNLA
     DLTHPIVIND EKEQALLSTL LQFEEAVLNV SREGQPHLMC TYLFELAGKF SSFYEACPIL
     NAEEAVKQSR LKLALLTAKT IKQGLDLLGI ETLERM
 
 
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